(data stored in SCRATCH zone)

SWISSPROT: Q13R20_PARXL

ID   Q13R20_PARXL            Unreviewed;       477 AA.
AC   Q13R20;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   07-JUN-2017, entry version 91.
DE   RecName: Full=3-isopropylmalate dehydratase large subunit {ECO:0000256|HAMAP-Rule:MF_01026};
DE            EC=4.2.1.33 {ECO:0000256|HAMAP-Rule:MF_01026};
DE   AltName: Full=Alpha-IPM isomerase {ECO:0000256|HAMAP-Rule:MF_01026};
DE            Short=IPMI {ECO:0000256|HAMAP-Rule:MF_01026};
DE   AltName: Full=Isopropylmalate isomerase {ECO:0000256|HAMAP-Rule:MF_01026};
GN   Name=leuC {ECO:0000256|HAMAP-Rule:MF_01026};
GN   ORFNames=Bxe_B2522 {ECO:0000313|EMBL:ABE33469.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE33469.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE33469.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE33469.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate
CC       and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
CC       {ECO:0000256|HAMAP-Rule:MF_01026, ECO:0000256|SAAS:SAAS00651872}.
CC   -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate = (2S)-2-
CC       isopropylmalate. {ECO:0000256|HAMAP-Rule:MF_01026,
CC       ECO:0000256|SAAS:SAAS00651862}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
CC       leucine from 3-methyl-2-oxobutanoate: step 2/4.
CC       {ECO:0000256|HAMAP-Rule:MF_01026, ECO:0000256|SAAS:SAAS00651850}.
CC   -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000256|HAMAP-
CC       Rule:MF_01026, ECO:0000256|SAAS:SAAS00651833}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC
CC       type 1 subfamily. {ECO:0000256|SAAS:SAAS00638189}.
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DR   EMBL; CP000271; ABE33469.1; -; Genomic_DNA.
DR   RefSeq; WP_011490837.1; NZ_CP008762.1.
DR   ProteinModelPortal; Q13R20; -.
DR   STRING; 266265.Bxe_B2522; -.
DR   EnsemblBacteria; ABE33469; ABE33469; Bxe_B2522.
DR   GeneID; 4006982; -.
DR   KEGG; bxb:DR64_4849; -.
DR   KEGG; bxe:Bxe_B2522; -.
DR   PATRIC; fig|266265.5.peg.5184; -.
DR   eggNOG; COG0065; LUCA.
DR   HOGENOM; HOG000226972; -.
DR   KO; K01703; -.
DR   OrthoDB; POG091H02GD; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000001817; Chromosome 2.
DR   GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   CDD; cd01583; IPMI; 1.
DR   Gene3D; 3.30.499.10; -; 2.
DR   Gene3D; 3.40.1060.10; -; 1.
DR   HAMAP; MF_01026; LeuC_type1; 1.
DR   InterPro; IPR004430; 3-IsopropMal_deHydase_lsu.
DR   InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR   InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR   InterPro; IPR015932; Aconitase/IPMdHydase_lsu_aba_2.
DR   InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR   InterPro; IPR033941; IPMI_cat.
DR   Pfam; PF00330; Aconitase; 1.
DR   PRINTS; PR00415; ACONITASE.
DR   SUPFAM; SSF53732; SSF53732; 1.
DR   TIGRFAMs; TIGR00170; leuC; 1.
DR   PROSITE; PS00450; ACONITASE_1; 1.
DR   PROSITE; PS01244; ACONITASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13R20.
DR   SWISS-2DPAGE; Q13R20.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01026,
KW   ECO:0000256|SAAS:SAAS00640307};
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01026,
KW   ECO:0000256|SAAS:SAAS00651837};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|HAMAP-
KW   Rule:MF_01026, ECO:0000256|SAAS:SAAS00651843};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01026, ECO:0000256|SAAS:SAAS00710141};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01026,
KW   ECO:0000256|SAAS:SAAS00710171};
KW   Leucine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01026,
KW   ECO:0000256|SAAS:SAAS00651868};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01026, ECO:0000256|SAAS:SAAS00638284,
KW   ECO:0000313|EMBL:ABE33469.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01026,
KW   ECO:0000256|SAAS:SAAS00710156};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   DOMAIN       10    462       Aconitase. {ECO:0000259|Pfam:PF00330}.
FT   METAL       349    349       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01026}.
FT   METAL       412    412       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01026}.
FT   METAL       415    415       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01026}.
SQ   SEQUENCE   477 AA;  51088 MW;  5688884096F7A3F2 CRC64;
     MTQPRTLYDR IFDAHVVRTD ADGTTLLYID RHLLNEVTSP QAFESLRREG RPVWRPQANL
     AVADHNVPTT DRRLGIADPV SRIQVDVLRE NCERSGIVHY GMDDARQGIV HVVGPELGCT
     LPGMTIVCGD SHTSTHGALG ALAFGIGTSE IEHVLGTQTL ITRRSRTMRM TLDGVLPPGC
     TAKDVALAVI GALGTAGGTG YAIEFAGPVV RALSMEGRMT LCNMSIEAGA RAGLIAVDET
     TLDYCRTRPH APQGETWELS ARVWRALRSD DDARFDAECS LDVSTLAPQV TWGTSPEMVT
     GIDGRVPDPL DIHDAGRRAS WQRALDYMGL DAGTRIDTIA IDKVFIGSCT NGRLEDLRAA
     ADILRATGGR IASNVRLALA VPGSQQVKRD AEAEGLHDVF IAAGFEWREP GCSMCLAMNP
     DRLEPGERVA STSNRNFEGR QGAGGRSHLV SPAMAAAAAL AGRFADVRPF ASGMGGL
//

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